Odorant coreceptor (Orco) represents one of the essential genes in the insect olfactory system, which facilitates signal transduction and heterodimerization with different odorant receptors (Ors) in the insect antennal dendritic membrane. Evolutionary analysis by detecting positive selection is important to examine the functional flexibility of Orco that potentially supports insect survival. The maximum likelihood codon substitution model was applied using CODEML program as implemented in PAML ver 4.9e package across 59 Orco codon sequences available from GenBank. These sequences represented five major insect orders and two reproductive systems (holometabola and nonholometabola). In the site model that identified common ω values for Orco, it was clearly shown that Orco was under strong purifying selection, indicated by the ω value that was far from 1 (ω: 0.03). However, in to the branch model, positive selection was detected to be acting on Dipteran lineages, whereas in the branch-site model, several sites were under significant positive selection occurring in the following four clades: Coleoptera, Diptera, Lepidoptera, and Psocodea. The typical evolutionary mode acting on Orco was consistent with the entropy value [H(x)], confirming that 48.9% of the Orco site was under conservation (H(x) < 0.5), whereas 26.9% of the Orco sites was under high variation (H(x) > 1). These findings confirmed that Orco genes are generally highly conserved and can possibly be used for the manipulation of insect pest control programs. However, positive selection that acts on certain lineages suggested future adaptive evolutionary ability of Orco to anticipate flexible functions for successful olfactory processes.
P5, one of the protein disulphide isomerase (PDI) family members, catalyses disulphide bond formation in proteins and exhibits molecular chaperone and calcium binding activities in vitro, whereas its physiological significance remains controversial. Recently, we have reported that P5 localizes not only in the ER but also in mitochondria, although it remains unclear so far about its physiological significance(s) of its dual localization. Here we report that H(2)O(2)- or rotenone-induced cell death is suppressed in MTS-P5 cells, which stably express P5 in mitochondria. H(2)O(2)-induced cell death in Saos-2 cells occurred, in large part, through caspase-independent and poly(ADP-ribose) polymerase (PARP)-dependent manner. In MTS-P5 cells challenged with H(2)O(2) treatment, PARP was still activated, whereas release of cytochrome c or apoptosis-inducing factor and intramitochondrial superoxide generation were suppressed. We also found that mitochondrial P5 was in close contact with citrate synthase and maintained large parts of its activity under H(2)O(2) exposure. These results suggest that mitochondrial P5 may upregulate tricarboxylic acid cycle and possibly, other intramitochondrial metabolism.
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